Ontology highlight
ABSTRACT:
SUBMITTER: Kong L
PROVIDER: S-EPMC3823233 | biostudies-literature | 2013 Jul
REPOSITORIES: biostudies-literature
Kong Leopold L Lee Jeong Hyun JH Doores Katie J KJ Murin Charles D CD Julien Jean-Philippe JP McBride Ryan R Liu Yan Y Marozsan Andre A Cupo Albert A Klasse Per-Johan PJ Hoffenberg Simon S Caulfield Michael M King C Richter CR Hua Yuanzi Y Le Khoa M KM Khayat Reza R Deller Marc C MC Clayton Thomas T Tien Henry H Feizi Ten T Sanders Rogier W RW Paulson James C JC Moore John P JP Stanfield Robyn L RL Burton Dennis R DR Ward Andrew B AB Wilson Ian A IA
Nature structural & molecular biology 20130526 7
A substantial proportion of the broadly neutralizing antibodies (bnAbs) identified in certain HIV-infected donors recognize glycan-dependent epitopes on HIV-1 gp120. Here we elucidate how the bnAb PGT 135 binds its Asn332 glycan-dependent epitope from its 3.1-Å crystal structure with gp120, CD4 and Fab 17b. PGT 135 interacts with glycans at Asn332, Asn392 and Asn386, using long CDR loops H1 and H3 to penetrate the glycan shield and access the gp120 protein surface. EM reveals that PGT 135 can ac ...[more]